Feb 13, 1976

Purification and some properties of rat liver cysteine oxidase (cysteine dioxygenase)

Biochimica Et Biophysica Acta
S SakakibaraI Ueda


Cysteine oxidase (cysteine dioxygenase, EC was purified approximately 1000-fold from rat liver. The purified enzyme (protein-B) was obtained as an inactive form, which was activated by anaerobic preincubation with L-cysteine. The active form of protein-B was inactivated during aerobic incubation to produce cysteine sulfinate. This inactivation of protein-B was protected by a distinct protein in rat liver cytoplasm, namely stabilizing protein (protein-A). The Ka and Km values for L-cysteine were 0.8-10(-3) M and 1.3-10(-3) M respectively. The enzyme was strongly inhibited by Cu+ and/or Fe2+ chelating agents but not by Cu2+ chelating agent. The optimum pH of enzyme reaction was 8.5-9.5 while that of enzyme activation was 6.8-9.5, with a broad peak.

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Mentioned in this Paper

Hydrogen-Ion Concentration
Cytoplasmic Matrix
Cysteine Hydrochloride

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